Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.
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Acetylation and phosphorylation control both local and global stability of the chloroplast F1 ATP synthaseIdentifying key membrane protein lipid interactions using mass spectrometry.The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.Lipid binding attenuates channel closure of the outer membrane protein OmpF
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Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 30 June 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Dimer interface of bovine cyto ...... difications and lipid binding.
@en
Dimer interface of bovine cyto ...... difications and lipid binding.
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type
label
Dimer interface of bovine cyto ...... difications and lipid binding.
@en
Dimer interface of bovine cyto ...... difications and lipid binding.
@nl
prefLabel
Dimer interface of bovine cyto ...... difications and lipid binding.
@en
Dimer interface of bovine cyto ...... difications and lipid binding.
@nl
P2860
P50
P356
P1476
Dimer interface of bovine cyto ...... difications and lipid binding.
@en
P2093
Idlir Liko
Shinya Yoshikawa
P2860
P304
P356
10.1073/PNAS.1600354113
P407
P577
2016-06-30T00:00:00Z